ID D5EUK2_PRER2 Unreviewed; 575 AA.
AC D5EUK2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ADE81868.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:ADE81868.1};
GN OrderedLocusNames=PRU_2034 {ECO:0000313|EMBL:ADE81868.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE81868.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE81868.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP002006; ADE81868.1; -; Genomic_DNA.
DR RefSeq; WP_013063855.1; NC_014033.1.
DR AlphaFoldDB; D5EUK2; -.
DR STRING; 264731.PRU_2034; -.
DR KEGG; pru:PRU_2034; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_10; -.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927}.
FT DOMAIN 93..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 173..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 452..563
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 575 AA; 64465 MW; D76C4ED7A8C8A469 CRC64;
MANYYSDHPE IGFYLNHPLM ARIVELKEKG FADAKEYDYA PVDLGDAIEN YKQILDITGD
VAANIIEPNS ESVDLEGPHL ENGRMIYASK TYENLDATRK AGLWGVSMPR RYGGLNLPNT
VFSMLSEMIS SADAGFQNIW SLQSCIDTLY EFGSEEQRQK YIPRVCAGEG MSMDLTEPDA
GSDLQRVMLK ATFDEKENCW RLNGVKRFIT NGDSDIHLVL ARSEEGTKDG RGLSMFIYDK
RQGGVDVRHI EHKLGIHGSP TCELTYKNAK AELCGSTRLG LIKYVMALMN GARLGIAAQS
VGVEQEAYNE GLAYAKERQQ FGDKIINFPA VYDMLSRMKA KLDAGRSLLY ETAAYVDIYK
CLEDIERDRK LTPEEKQELK KYQRLADAFT PLAKGMNSEY ANQNAYDAIS IHGGSGFIME
YKSQRLFRDA RIFSIYEGTT QLQVVAAIRY ITNGTMLNNI KDMLAALPAE ANAALKARVE
KLIPVYEEAL AAVKALDNQD AHDFLARRLY DMTAELVMSL LILRDAAKAP ELFAKSANVY
VRMAEEDILG KAAYIKAFQV EDLENFRAND EETAE
//
